Seo Young Ho
College of Pharmacy, Keimyung University, Daegu, 704-701, Korea.
Arch Pharm Res. 2015 Oct;38(10):1783-8. doi: 10.1007/s12272-015-0595-6. Epub 2015 Apr 9.
Heat shock protein 90 (Hsp90) is a ATP dependent molecular chaperone and has emerged as an attractive therapeutic target in the war on cancer due to its role in regulating maturation and stabilization of numerous oncogenic proteins. In this study, we discovered that 2',4'-dimethoxychalcone (1b) disrupted Hsp90 chaperoning function and inhibited the growth of iressa-resistant non-small cell lung cancer (NSCLC, H1975). The result suggested that 2',4'-dimethoxychalcone (1b) could serve as a potential therapeutic lead to circumvent the drug resistance acquired by EGFR mutation and Met amplification.
热休克蛋白90（Hsp90）是一种依赖ATP的分子伴侣，由于其在调节众多致癌蛋白的成熟和稳定性方面的作用，已成为抗癌战争中一个有吸引力的治疗靶点。在本研究中，我们发现2'，4'-二甲氧基查耳酮（1b）破坏了Hsp90的伴侣功能，并抑制了对易瑞沙耐药的非小细胞肺癌（NSCLC，H1975）的生长。结果表明，2'，4'-二甲氧基查耳酮（1b）可作为一种潜在的治疗先导物，以规避由EGFR突变和Met扩增获得的耐药性。
